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TTR cDNA ORF clone, Homo sapiens (human)

Gene Symbol TTR
Entrez Gene ID 7276
Full Name transthyretin
Synonyms CTS, CTS1, HEL111, HsT2651, PALB, TBPA
General protein information
Preferred Names
transthyretin
Names
transthyretin
ATTR
carpal tunnel syndrome 1
thyroxine-binding prealbumin
prealbumin, amyloidosis type I
Gene Type protein-coding
Organism Homo sapiens (human)
Genome

18

18q12.1

Summary This gene encodes transthyretin, one of the three prealbumins including alpha-1-antitrypsin, transthyretin and orosomucoid. Transthyretin is a carrier protein; it transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. The protein consists of a tetramer of identical subunits. More than 80 different mutations in this gene have been reported; most mutations are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart, and a small portion of the gene mutations is non-amyloidogenic. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, carpal tunnel syndrome, etc. [provided by RefSeq, Jan 2009]. lac of sum
Disorder MIM:

176300

Disorder Html: Amyloidosis, hereditary, transthyretin-related, 105210 (3);

mRNA and Protein(s)

mRNA Protein Name
NM_000371 NP_000362 transthyretin precursor



Homo sapiens (human) TTR NP_000362.1
Pan troglodytes (chimpanzee) TTR NP_001009137.1
Macaca mulatta (Rhesus monkey) TTR XP_001099005.1
Canis lupus familiaris (dog) TTR XP_537290.1
Bos taurus (cattle) TTR NP_776392.1
Mus musculus (house mouse) Ttr NP_038725.1
Rattus norvegicus (Norway rat) Ttr NP_036813.2
Gallus gallus (chicken) TTR NP_990666.1
Danio rerio (zebrafish) ttr NP_001005598.2
Xenopus (Silurana) tropicalis (western clawed frog) ttr NP_001096539.1


GeneRIFs: Gene References Into Functions What's a GeneRIF?

The following TTR gene cDNA ORF clone sequences were retrieved from the NCBI Reference Sequence Database (RefSeq). These sequences represent the protein coding region of the TTR cDNA ORF which is encoded by the open reading frame (ORF) sequence. ORF sequences can be delivered in our standard vector, pcDNA3.1+/C-(K)DYK or the vector of your choice as an expression/transfection-ready ORF clone. Not the clone you want? Click here to find your clone.

***CloneID RefSeq Accession Definition **Vector *Turnaround time Price Select
OHu27033
NM_000371 Homo sapiens transthyretin (TTR), mRNA. pcDNA3.1+/C-(K)DYK or customized vector
in pcDNA3.1+/C-(K)DYK
$49.50-$69.30
$99.00
Next-day Shipping ORF Clones ( in default vector with tag)
1 Clone 30% OFF
2-4 Clone 40% OFF
5 or more Clone 50% OFF
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30% OFF

*Business Day

** You may select a custom vector to replace pcDNA3.1+/C-(K)DYK after clone is added to cart.

** GenScript guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories. In addition, please pay attention to the signal peptide, propeptide and transit peptide in target ORF, which may affect the choice of vector (N/C terminal tag vector).

***One clone ID might be correlated to multiple accession numbers, which share the same CDS sequence.


CloneID OHu27033
Clone ID Related Accession (Same CDS sequence) NM_000371
Accession Version NM_000371.3 Documents for ORF clone product in dufault vector
Sequence Information ORF Nucleotide Sequence (Length: 444bp)
Protein sequence
SNP
Vector pcDNA3.1+/C-(K)DYK or customized vector User Manual
Clone information Clone Map MSDS
Tag on pcDNA3.1+/C-(K)DYK C terminal DYKDDDDK tags COA
ORF Insert Method CloneEZ® Seamless cloning technology
Structure linear
Update Date 15-MAR-2015
Organism Homo sapiens (human)
Product transthyretin precursor
Comment REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from DB498675.1, BC020791.1 and CA948224.1. This sequence is a reference standard in the RefSeqGene project. On Jan 22, 2009 this sequence version replaced gi:167736363. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BI549547.1, CD357987.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968540, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## COMPLETENESS: complete on the 3' end.

1
61
121
181
241
301
361
421
ATGGCTTCTC ATCGTCTGCT CCTCCTCTGC CTTGCTGGAC TGGTATTTGT GTCTGAGGCT 
GGCCCTACGG GCACCGGTGA ATCCAAGTGT CCTCTGATGG TCAAAGTTCT AGATGCTGTC
CGAGGCAGTC CTGCCATCAA TGTGGCCGTG CATGTGTTCA GAAAGGCTGC TGATGACACC
TGGGAGCCAT TTGCCTCTGG GAAAACCAGT GAGTCTGGAG AGCTGCATGG GCTCACAACT
GAGGAGGAAT TTGTAGAAGG GATATACAAA GTGGAAATAG ACACCAAATC TTACTGGAAG
GCACTTGGCA TCTCCCCATT CCATGAGCAT GCAGAGGTGG TATTCACAGC CAACGACTCC
GGCCCCCGCC GCTACACCAT TGCCGCCCTG CTGAGCCCCT ACTCCTATTC CACCACGGCT
GTCGTCACCA ATCCCAAGGA ATGA

The stop codons will be deleted if pcDNA3.1+/C-(K)DYK vector is selected.

RefSeq NP_000362.1
CDS137..580
Misc Feature(1)83..85(+)
Misc Feature(2)206..568(+)
Misc Feature(3)239..553(+)
Misc Feature(4)251..562(+)
Misc Feature(5)320..322(+)
Misc Feature(6)539..553(+)
Exon (1)1..205
Gene:TTR
Gene Synonym:
Exon (2)206..336
Gene:TTR
Gene Synonym:
Exon (3)337..472
Gene:TTR
Gene Synonym:
Exon (4)473..929
Gene:TTR
Gene Synonym:
Translation

Target ORF information:

RefSeq Version NM_000371
Organism Homo sapiens (human)
Definition Homo sapiens transthyretin (TTR), mRNA.

Target ORF information:

Epitope DYKDDDDK
Bacterial selection AMPR
Mammalian selection NeoR
Vector pcDNA3.1+/C-(K)DYK
NM_000371

ORF Insert Sequence:

1
61
121
181
241
301
361
421
ATGGCTTCTC ATCGTCTGCT CCTCCTCTGC CTTGCTGGAC TGGTATTTGT GTCTGAGGCT 
GGCCCTACGG GCACCGGTGA ATCCAAGTGT CCTCTGATGG TCAAAGTTCT AGATGCTGTC
CGAGGCAGTC CTGCCATCAA TGTGGCCGTG CATGTGTTCA GAAAGGCTGC TGATGACACC
TGGGAGCCAT TTGCCTCTGG GAAAACCAGT GAGTCTGGAG AGCTGCATGG GCTCACAACT
GAGGAGGAAT TTGTAGAAGG GATATACAAA GTGGAAATAG ACACCAAATC TTACTGGAAG
GCACTTGGCA TCTCCCCATT CCATGAGCAT GCAGAGGTGG TATTCACAGC CAACGACTCC
GGCCCCCGCC GCTACACCAT TGCCGCCCTG CTGAGCCCCT ACTCCTATTC CACCACGGCT
GTCGTCACCA ATCCCAAGGA ATGA

The stop codons will be deleted if pcDNA3.1+/C-(K)DYK vector is selected.

book

Quantification of transthyretin kinetic stability in human plasma using subunit exchange
Biochemistry 53 (12), 1993-2006 (2014)
Rappley I, Monteiro C, Novais M, Baranczak A, Solis G, Wiseman RL, Helmke S, Maurer MS, Coelho T, Powers ET and Kelly JW.


book

Proteolytic cleavage of Ser52Pro variant transthyretin triggers its amyloid fibrillogenesis
Proc. Natl. Acad. Sci. U.S.A. 111 (4), 1539-1544 (2014)
Mangione PP, Porcari R, Gillmore JD, Pucci P, Monti M, Porcari M, Giorgetti S, Marchese L, Raimondi S, Serpell LC, Chen W, Relini A, Marcoux J, Clatworthy IR, Taylor GW, Tennent GA, Robinson CV, Hawkins PN, Stoppini M, Wood SP, Pepys MB and Bellotti V.


book

Transthyretin proteins regulate angiogenesis by conferring different molecular identities to endothelial cells
J. Biol. Chem. 288 (44), 31752-31760 (2013)
Nunes RJ, de Oliveira P, Lages A, Becker JD, Marcelino P, Barroso E, Perdigoto R, Kelly JW, Quintas A and Santos SC.


book

Mutation p.G83R in the transthyretin gene is associated with hereditary vitreous amyloidosis in Han Chinese families
Mol. Vis. 19, 1631-1638 (2013)
Zhang AM, Wang H, Sun P, Hu QX, He Y and Yao YG.


book

Unexplained cardiac failure leading to the identification of a Belgian family affected by hereditary amyloidosis
Acta Clin Belg 68 (4), 303-305 (2013)
De Pasqual A, Biessaux Y, Blettard N, Cremers S and Caers J.


book

Familial Transthyretin Amyloidosis
(in) Pagon RA, Adam MP, Ardinger HH, Bird TD, Dolan CR, Fong CT, Smith RJH and Stephens K (Eds.); GENEREVIEWS(R); (1993)
Sekijima,Y., Yoshida,K., Tokuda,T. and Ikeda,S.


book

Interaction between prealbumin and retinol-binding protein studied by affinity chromatography, gel filtration and two-phase partition
Eur. J. Biochem. 99 (2), 353-360 (1979)
Fex,G., Albertsson,P.A. and Hansson,B.


book

Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A
J. Mol. Biol. 121 (3), 339-356 (1978)
Blake,C.C., Geisow,M.J., Oatley,S.J., Rerat,B. and Rerat,C.


book

Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor?
Nature 268 (5616), 115-120 (1977)
Blake,C.C. and Oatley,S.J.


book

The interaction between retinol-binding proteins and prealbumins studied by fluorescence polarization
Biochim. Biophys. Acta 439 (2), 449-460 (1976)
Kopelman,M., Cogan,U., Mokady,S. and Shinitzky,M.


 
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